ID   SYRC_YEAST              Reviewed;         607 AA.
AC   Q05506; D6VSX2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Arginine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   OrderedLocusNames=YDR341C; ORFNames=D9651.10;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8] {ECO:0007744|PDB:1BS2}
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH L-ARGININE, AND
RP   SUBUNIT.
RX   PubMed=9736621; DOI=10.1093/emboj/17.18.5438;
RA   Cavarelli J., Delagoutte B., Eriani G., Gangloff J., Moras D.;
RT   "L-arginine recognition by yeast arginyl-tRNA synthetase.";
RL   EMBO J. 17:5438-5448(1998).
RN   [9] {ECO:0007744|PDB:1F7U, ECO:0007744|PDB:1F7V}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH L-ARGININE AND RNA.
RX   PubMed=11060012; DOI=10.1093/emboj/19.21.5599;
RA   Delagoutte B., Moras D., Cavarelli J.;
RT   "tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations
RT   during substrates binding.";
RL   EMBO J. 19:5599-5610(2000).
CC   -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC       attachment of specific amino acids to cognate tRNAs during protein
CC       synthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9736621}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
CC   -!- MISCELLANEOUS: Present with 20600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; U51032; AAB64777.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12182.1; -; Genomic_DNA.
DR   PIR; S70106; S70106.
DR   RefSeq; NP_010628.3; NM_001180649.3.
DR   PDB; 1BS2; X-ray; 2.75 A; A=1-607.
DR   PDB; 1F7U; X-ray; 2.20 A; A=1-607.
DR   PDB; 1F7V; X-ray; 2.90 A; A=1-607.
DR   PDBsum; 1BS2; -.
DR   PDBsum; 1F7U; -.
DR   PDBsum; 1F7V; -.
DR   AlphaFoldDB; Q05506; -.
DR   SMR; Q05506; -.
DR   BioGRID; 32398; 158.
DR   DIP; DIP-5046N; -.
DR   IntAct; Q05506; 4.
DR   STRING; 4932.YDR341C; -.
DR   iPTMnet; Q05506; -.
DR   MaxQB; Q05506; -.
DR   PaxDb; 4932-YDR341C; -.
DR   PeptideAtlas; Q05506; -.
DR   TopDownProteomics; Q05506; -.
DR   EnsemblFungi; YDR341C_mRNA; YDR341C; YDR341C.
DR   GeneID; 851942; -.
DR   KEGG; sce:YDR341C; -.
DR   AGR; SGD:S000002749; -.
DR   SGD; S000002749; YDR341C.
DR   VEuPathDB; FungiDB:YDR341C; -.
DR   eggNOG; KOG1195; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; CLU_006406_6_2_1; -.
DR   InParanoid; Q05506; -.
DR   OMA; YEFKWER; -.
DR   OrthoDB; 67085at2759; -.
DR   BioCyc; YEAST:G3O-29896-MONOMER; -.
DR   BRENDA; 6.1.1.19; 984.
DR   BioGRID-ORCS; 851942; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q05506; -.
DR   PRO; PR:Q05506; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q05506; Protein.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   CDD; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW   Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..607
FT                   /note="Arginine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000151664"
FT   REGION          59..60
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000269|PubMed:11060012"
FT   REGION          106..111
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000269|PubMed:11060012"
FT   REGION          484..498
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000269|PubMed:11060012"
FT   MOTIF           151..162
FT                   /note="'HIGH' region"
FT   BINDING         148..153
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000269|PubMed:11060012,
FT                   ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT                   ECO:0007744|PDB:1F7U"
FT   BINDING         162
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000269|PubMed:9736621,
FT                   ECO:0007744|PDB:1BS2"
FT   BINDING         347
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000269|PubMed:11060012,
FT                   ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT                   ECO:0007744|PDB:1F7U"
FT   BINDING         351
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000269|PubMed:11060012,
FT                   ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT                   ECO:0007744|PDB:1F7U"
FT   BINDING         375
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000269|PubMed:11060012,
FT                   ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2,
FT                   ECO:0007744|PDB:1F7U"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           31..47
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           83..92
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           116..130
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           163..178
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          182..190
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           194..206
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           216..233
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          235..238
FT                   /evidence="ECO:0007829|PDB:1BS2"
FT   TURN            240..242
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           246..257
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           260..283
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           299..311
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          315..318
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          321..325
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           326..328
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   TURN            331..333
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          335..339
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   TURN            341..343
FT                   /evidence="ECO:0007829|PDB:1BS2"
FT   HELIX           347..362
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           373..375
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           376..388
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           392..396
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          397..400
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          405..407
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   TURN            410..413
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           418..434
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           437..440
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           446..463
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           475..479
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   STRAND          482..485
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           486..502
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   TURN            503..505
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           508..511
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           516..518
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           522..531
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           534..544
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           547..567
FT                   /evidence="ECO:0007829|PDB:1F7U"
FT   HELIX           575..599
FT                   /evidence="ECO:0007829|PDB:1F7U"
SQ   SEQUENCE   607 AA;  69525 MW;  8349ABC0E30E50F1 CRC64;
     MASTANMISQ LKKLSIAEPA VAKDSHPDVN IVDLMRNYIS QELSKISGVD SSLIFPALEW
     TNTMERGDLL IPIPRLRIKG ANPKDLAVQW AEKFPCGDFL EKVEANGPFI QFFFNPQFLA
     KLVIPDILTR KEDYGSCKLV ENKKVIIEFS SPNIAKPFHA GHLRSTIIGG FLANLYEKLG
     WEVIRMNYLG DWGKQFGLLA VGFERYGNEE ALVKDPIHHL FDVYVRINKD IEEEGDSIPL
     EQSTNGKARE YFKRMEDGDE EALKIWKRFR EFSIEKYIDT YARLNIKYDV YSGESQVSKE
     SMLKAIDLFK EKGLTHEDKG AVLIDLTKFN KKLGKAIVQK SDGTTLYLTR DVGAAMDRYE
     KYHFDKMIYV IASQQDLHAA QFFEILKQMG FEWAKDLQHV NFGMVQGMST RKGTVVFLDN
     ILEETKEKMH EVMKKNENKY AQIEHPEEVA DLVGISAVMI QDMQGKRINN YEFKWERMLS
     FEGDTGPYLQ YAHSRLRSVE RNASGITQEK WINADFSLLK EPAAKLLIRL LGQYPDVLRN
     AIKTHEPTTV VTYLFKLTHQ VSSCYDVLWV AGQTEELATA RLALYGAARQ VLYNGMRLLG
     LTPVERM
//